3wws

X-ray diffraction
2.01Å resolution

Crystal structure of Serine/threonine-protein kinase 3

Released:
Source organism: Homo sapiens
Entry authors: Lee SJ, Song J, Yamashita E

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-171589 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase 3 20kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 51 amino acids
Theoretical weight: 6.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13188 (Residues: 436-484; Coverage: 10%)
Gene names: KRS1, MST2, STK3
Sequence domains: C terminal SARAH domain of Mst1
Structure domains: p53-like tetramerisation domain
Serine/threonine-protein kinase 3 20kDa subunit Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 49 amino acids
Theoretical weight: 6.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13188 (Residues: 436-484; Coverage: 10%)
Gene names: KRS1, MST2, STK3
Sequence domains: C terminal SARAH domain of Mst1
Structure domains: p53-like tetramerisation domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 128.831Å b: 32.678Å c: 55.83Å
α: 90° β: 109.63° γ: 90°
R-values:
R R work R free
0.271 0.269 0.311
Expression system: Escherichia coli